ID   A0A183CFZ8_GLOPA        Unreviewed;      1117 AA.
AC   A0A183CFZ8;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 32.
DE   SubName: Full=BED-type domain-containing protein {ECO:0000313|WBParaSite:GPLIN_001180300};
OS   Globodera pallida (Potato cyst nematode).
OC   Eukaryota; Metazoa; Ecdysozoa; Nematoda; Chromadorea; Rhabditida;
OC   Tylenchina; Tylenchomorpha; Tylenchoidea; Heteroderidae; Heteroderinae;
OC   Globodera.
OX   NCBI_TaxID=36090 {ECO:0000313|Proteomes:UP000050741, ECO:0000313|WBParaSite:GPLIN_001180300};
RN   [1] {ECO:0000313|Proteomes:UP000050741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA   Aslett M.;
RL   Submitted (DEC-2013) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000050741}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Lindley {ECO:0000313|Proteomes:UP000050741};
RA   Cotton J.A., Lilley C.J., Jones L.M., Kikuchi T., Reid A.J., Thorpe P.,
RA   Tsai I.J., Beasley H., Blok V., Cock P.J.A., Van den Akker S.E.,
RA   Holroyd N., Hunt M., Mantelin S., Naghra H., Pain A., Palomares-Rius J.E.,
RA   Zarowiecki M., Berriman M., Jones J.T., Urwin P.E.;
RT   "The genome and life-stage specific transcriptomes of Globodera pallida
RT   elucidate key aspects of plant parasitism by a cyst nematode.";
RL   Submitted (MAY-2014) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|WBParaSite:GPLIN_001180300}
RP   IDENTIFICATION.
RG   WormBaseParasite;
RL   Submitted (JUN-2016) to UniProtKB.
CC   -!- SUBUNIT: Collagen polypeptide chains are complexed within the cuticle
CC       by disulfide bonds and other types of covalent cross-links.
CC       {ECO:0000256|ARBA:ARBA00011518}.
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DR   AlphaFoldDB; A0A183CFZ8; -.
DR   WBParaSite; GPLIN_001180300; GPLIN_001180300; GPLIN_001180300.
DR   Proteomes; UP000050741; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0048856; P:anatomical structure development; IEA:UniProt.
DR   InterPro; IPR008160; Collagen.
DR   PANTHER; PTHR24637; COLLAGEN; 1.
DR   PANTHER; PTHR24637:SF354; COLLAGEN; 1.
DR   Pfam; PF01391; Collagen; 2.
PE   4: Predicted;
KW   Disulfide bond {ECO:0000256|ARBA:ARBA00023157};
KW   Membrane {ECO:0000256|SAM:Phobius}; Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        669..693
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   TRANSMEM        802..825
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   REGION          1..26
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          92..115
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          634..660
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          907..938
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          960..1083
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        642..660
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1019..1033
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1117 AA;  122722 MW;  DC4B1ED901FE2DB5 CRC64;
     MGSIGCEATT VDEHEHQQND AGADSSDNSA NAINLWQICP FLFEASSSPG GGSVRCTECG
     DSEQFNDLGS TYNHLKKRHP QQFQQLYEQW KREPPPKRRP HMAKQQNAKR NGGNARVSVN
     IELQETAFVD PSTFICGQQQ NCSENEPKQG PAPAGVWCVG LFERHHFRNG TVGALCLECG
     QMLWELDTDV ELMRHLVDKH PEYMPNLTAN VPSSTDQQNV PTYIDEQGEL WQCLDIANNG
     ESAEEMFHRH GARPVQQQQQ QLGGLFGLDN AEKFLLCCAF DASLLCSFRA IWIGHQRAIF
     QSLGHNHRII GETCAINAGS TSTSSPGVSV NIELQETAFV DPSTFICGQQ QNCSENEPKQ
     GPAPAGVWCV GLFERHHFRN GTVGALCLEC GQMLWELDTD AELMRHLVDK HPEYMPNLTA
     NVPSSTDQQN VPTYIDEQGE LWQCLDIANN GESAEEMFHR HGARPVQQQQ QQLGGLFGLD
     NAEKFLLCCA FDASLFSPES VMETIERVLQ QDHSTFVDAG GKEWHWLADV SASGGEAELR
     RACRAHDLYR EGGARNFSCK WSSRNARSSF NCPLRGLYVP QRNALFYRQN HNHSLPVTAP
     PKNNGMVRRN SLEMNSASSP GTCCAQSSFR SLPVAQNRRP RHQQHPLGEG EQYKQEEEEE
     RGRENAYKAV LVLSLCFSLC AWTCILTVCP LLYQLISFTT SQFDGILQFC EDTAQTVATE
     SAGLMEMFSR EHQYAEDDGV DQSQVGGVNR TRSRNFRHVL PLHFQHQLQE QENGCRSIRS
     GGRADKQQEE EERGRENAYK AVLVLSLCFS LCAWTCILTV CPLLYQLISF TTSQFDGILQ
     FCEDTAQTVA TESAGLMEMF SREHQYAEDD GVDQSQVGGV NRTRSRNFRH VLPLHFQHQL
     QEQENGCRCA PESGPQGTPG RMGMKGTPGA KGAPGLPARL PCEPLQDLKK FCPEKCPQGL
     QGQSGFRGSH GEKGRPGPIG LSGKNGEDGK TGPRGMPGPP GVPGLDGEDG ESGTDAQPMP
     FVPGPPGPAG EIGDSGPPGP RGLPGIDGTQ GPQGRKGAQG NAGKMGSSGT PGPTGPIGEP
     GEDGHKGVCP TYCAMDGGVF FVEPPEWFFK NSQKKRK
//